Results 11 to 20 of about 19,027,943 (182)

Cell-Free and In Vivo Characterization of the Inhibitory Activity of Lavado Cocoa Flavanols on the Amyloid Protein Ataxin-3: Toward New Approaches against Spinocerebellar Ataxia Type 3. [PDF]

ACS Chem Neurosci, 2023
Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder characterized by ataxia and other neurological manifestations, with a poor prognosis and a lack of effective therapies.
Sciandrone B, Palmioli A, Ciaramelli C, Pensotti R, Colombo L, Regonesi ME, Airoldi C.   +6 more
europepmc   +2 more sources

Ubiquitin-binding site 1 of pathogenic ataxin-3 regulates its toxicity in <i>Drosophila</i> models of Spinocerebellar Ataxia Type 3. [PDF]

Front Neurosci, 2022
Spinocerebellar Ataxia Type 3 (SCA3) is a member of the family of polyglutamine (polyQ) diseases that are caused by anomalous CAG triplet repeat expansions in several genes. SCA3 results from abnormal polyQ expansion in the deubiquitinase (DUB), ataxin-3
Prifti MV, Libohova K, Harris AL, Tsou WL, Todi SV.   +4 more
europepmc   +2 more sources

Label-free autofluorescence lifetime reveals the structural dynamics of ataxin-3 inside droplets formed via liquid-liquid phase separation. [PDF]

Sci Rep, 2023
Liquid–liquid phase separation is a phenomenon that features the formation of liquid droplets containing concentrated solutes. The droplets of neurodegeneration-associated proteins are prone to generate aggregates and cause diseases.
Matsuura U, Tahara S, Kajimoto S, Nakabayashi T.   +3 more
europepmc   +2 more sources

Ataxin-3 Overexpression via Adeno-associated Viral Vector Injection in the Primate Cerebellum: A Novel Model of Spinocerebellar Ataxia Type 3. [PDF]

Exp Neurobiol
Spinocerebellar ataxia type 3 (SCA3) is an autosomal-dominant neurodegenerative disorder caused by an expanded polyglutamine repeat in the ataxin-3 gene.
Kim K, Kim A, Won J, Park J, Lim KS, Jeon CY, Min J, Cho JH, Song Y, Koo BS, Bae GS, Jeon E, Jeong KJ, Park SH, Lee HY, Choi WS, Lee DS, Lee Y.   +17 more
europepmc   +2 more sources

KPNB1 modulates the Machado-Joseph disease protein ataxin-3 through activation of the mitochondrial protease CLPP. [PDF]

Cell Mol Life Sci, 2022
Machado–Joseph disease (MJD) is characterized by a pathological expansion of the polyglutamine (polyQ) tract within the ataxin-3 protein. Despite its primarily cytoplasmic localization, polyQ-expanded ataxin-3 accumulates in the nucleus and forms ...
Abeditashi M, Weber JJ, Pereira Sena P, Velic A, Kalimeri M, Incebacak Eltemur RD, Schmidt J, Hübener-Schmid J, Hauser S, Macek B, Riess O, Schmidt T.   +11 more
europepmc   +2 more sources

The deubiquitinase function of ataxin-3 and its role in the pathogenesis of Machado-Joseph disease and other diseases. [PDF]

Biochem J
Machado-Joseph disease (MJD) is a devastating and incurable neurodegenerative disease characterised by progressive ataxia, difficulty speaking and swallowing.
Potapenko A, Davidson JM, Lee A, Laird AS.   +3 more
europepmc   +2 more sources

Evolutionary model of repeat insertions in Ataxin-3 traces the origin of the polyglutamine stretch to an ancestral ubiquitin binding module. [PDF]

Protein Sci
The human ataxin‐3 protein contains an N‐terminal Josephin domain, composed of a papain‐like cysteine protease with a helical hairpin insertion, and a C‐terminal region with two or three ubiquitin interacting motifs and a polyglutamine tract.
Felício D, Martins S, Alves GP, Amorim A, Macedo-Ribeiro S, Merski M.   +5 more
europepmc   +2 more sources

Roles of orexinergic and noradrenergic neuronal activity in ketamine-induced sedation: a study using an orexin-ataxin-3 transgenic rat model. [PDF]

J Anesth
To investigate the role of brain noradrenergic and orexinergic activity in ketamine-induced sedation. We used orexin neuron-deficient transgenic rats (orexin/ataxin-3) and wild-type controls.
Tonosaki M, Kushikata T, Nikaido Y, Takekawa D, Kinoshita H, Saito J, Hirota K.   +6 more
europepmc   +2 more sources

Roles of orexinergic and noradrenergic neuronal activity in ketamine-induced analgesia: A study using an orexin/ataxin-3 transgenic rat model. [PDF]

J Anesth Transl Med
Background Orexin, a neuropeptide, physiologically interacts with locus coeruleus noradrenergic (LC-NA) activity. We hypothesized that this interaction affects ketamine-induced acute analgesia.
Tonosaki M, Kushikata T, Nikaido Y, Takekawa D, Kinoshita H, Saito J, Hirota K.   +6 more
europepmc   +2 more sources

PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates. [PDF]

Sci Rep, 2021
Polyglutamine (polyQ) expansion of proteins can trigger protein misfolding and amyloid-like aggregation, which thus lead to severe cytotoxicities and even the respective neurodegenerative diseases.
Yue HW, Hong JY, Zhang SX, Jiang LL, Hu HY.   +4 more
europepmc   +2 more sources